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In chemistry, an amphiphile (from Greek αμφις (amphis) 'both' and φιλíα 'love, friendship'), or amphipath, is a chemical compound possessing both hydrophilic (water-loving, polar) and lipophilic (fat-loving, nonpolar) properties. [1] Such a compound is called amphiphilic or amphipathic.
Biological molecules are amphiphilic or amphipathic, i.e. are simultaneously hydrophobic and hydrophilic. [6] The phospholipid bilayer contains charged hydrophilic headgroups, which interact with polar water. The layers also contain hydrophobic tails, which meet with the hydrophobic tails of the complementary layer.
Glycerophospholipids are the main structural component of biological membranes. Their amphipathic nature drives the formation of the lipid bilayer structure of membranes. The cell membrane seen under the electron microscope consists of two identifiable layers, or "leaflets", each of which is made up of an ordered row of glycerophospholipid ...
[citation needed] The glycerophospholipids are amphipathic molecules (containing both hydrophobic and hydrophilic regions) that contain a glycerol core linked to two fatty acid-derived "tails" by ester linkages and to one "head" group by a phosphate ester linkage.
In water, the hydrophilic "heads" of surfactant molecules are always in contact with the solvent, regardless of whether the surfactants exist as monomers or as part of a micelle. However, the lipophilic "tails" of surfactant molecules have less contact with water when they are part of a micelle—this being the basis for the energetic drive for ...
Hydrophilic molecules (and portions of molecules) can be contrasted with hydrophobic molecules (and portions of molecules). In some cases, both hydrophilic and hydrophobic properties occur in a single molecule. An example of these amphiphilic molecules is the lipids that comprise the cell membrane. Another example is soap, which has a ...
The aromatic/arginine or "ar/R" selectivity filter is a cluster of amino acids that help bind to water molecules and exclude other molecules that may try to enter the pore. It is the mechanism by which the aquaporin is able to selectively bind water molecules and so to allow them through, and to prevent other molecules from entering.
Therefore, the hydrophobic interaction between the hydrophobic face of amphipathic antimicrobial peptides and the zwitterionic phospholipids on the cell surface of mammalian cell membranes plays a major role in the formation of peptide-cell binding.